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Characterisation of the interface between nucleophosmin (NPM) and p53: Potential role in p53 stabilisation
Author(s) -
Lambert B.,
Buckle M.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.025
Subject(s) - nucleophosmin , surface plasmon resonance , dna damage repair , chemistry , mass spectrometry , biophysics , peptide , stoichiometry , protein–protein interaction , biochemistry , dna , dna damage , biology , nanotechnology , materials science , chromatography , nanoparticle , gene
We have used surface plasmon resonance to quantify the kinetics and stoichiometry of the interaction between p53 and nucleophosmin (NPM). Domains characterising the interface between the two proteins were identified by chemical cross‐linking, proteolytic digestion and mass spectrometry based peptide mapping.We show that the C‐terminal domain of NPM (residues 242–269) interacts with two regions of p53 (residues 175–196 and residues 343–363) which belong, respectively, to the DNA binding domain and the tetramerisation domain. Potential biological consequences of such interactions are discussed.